Zinc in PDB 2f9i: Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus

The structure of Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus, PDB code: 2f9i was solved by P.W.Bilder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.98
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	190.979, 50.859, 149.639, 90.00, 113.51, 90.00
R / Rfree (%)	18.6 / 21.3

The binding sites of Zinc atom in the Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus (pdb code 2f9i). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus, PDB code: 2f9i:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:35.9 occ:1.00 SG B:CYS55 2.2 36.1 1.0 SG B:CYS33 2.2 38.3 1.0 SG B:CYS52 2.2 36.1 1.0 SG B:CYS36 2.4 39.5 1.0 CB B:CYS33 3.1 42.0 1.0 CB B:CYS52 3.2 37.2 1.0 CB B:CYS55 3.3 39.7 1.0 CB B:CYS36 3.4 44.5 1.0 N B:CYS36 3.7 46.0 1.0 N B:CYS55 3.8 40.6 1.0 CA B:CYS55 4.1 40.0 1.0 CA B:CYS36 4.1 44.4 1.0 CB B:HIS57 4.3 36.1 1.0 CA B:CYS33 4.6 42.1 1.0 C B:CYS55 4.6 39.1 1.0 CA B:CYS52 4.6 37.8 1.0 CB B:ASN54 4.7 41.4 1.0 N B:HIS57 4.7 36.7 1.0 C B:ASN54 4.7 41.5 1.0 N B:ASP56 4.7 39.1 1.0 CB B:LYS35 4.8 47.9 1.0 C B:LYS35 4.8 46.8 1.0 C B:CYS36 4.8 44.1 1.0 N B:LYS37 5.0 43.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Carboxyltransferase Subunit of Acc From Staphylococcus Aureus within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn602 b:44.9 occ:1.00 SG D:CYS52 2.2 42.0 1.0 SG D:CYS33 2.3 47.8 1.0 SG D:CYS55 2.3 44.3 1.0 SG D:CYS36 2.4 49.5 1.0 CB D:CYS33 3.1 48.9 1.0 CB D:CYS52 3.1 39.7 1.0 CB D:CYS55 3.3 42.4 1.0 CB D:CYS36 3.4 51.5 1.0 N D:CYS55 3.6 48.5 0.0 N D:CYS36 3.9 53.2 1.0 CA D:CYS55 4.0 42.5 1.0 CA D:CYS36 4.2 52.1 1.0 CB D:HIS57 4.3 36.9 1.0 CB D:ASN54 4.5 45.7 1.0 CA D:CYS52 4.5 40.3 1.0 CA D:CYS33 4.5 49.4 1.0 C D:CYS55 4.6 41.4 1.0 ND2 D:ASN54 4.7 49.5 1.0 C D:ASN54 4.7 45.0 1.0 N D:HIS57 4.7 38.0 1.0 N D:ASP56 4.8 41.1 1.0 C D:CYS36 4.8 52.0 1.0 CB D:LYS38 4.9 49.0 1.0 N D:LYS37 5.0 51.5 1.0 N D:ASN54 5.0 44.4 1.0 CA D:ASN54 5.0 45.0 1.0

P.Bilder, S.Lightle, G.Bainbridge, J.Ohren, B.Finzel, F.Sun, S.Holley, L.Al-Kassim, C.Spessard, M.Melnick, M.Newcomer, G.L.Waldrop. The Structure of the Carboxyltransferase Component of Acetyl-Coa Carboxylase Reveals A Zinc-Binding Motif Unique to the Bacterial Enzyme. Biochemistry V. 45 1712 2006.
ISSN: ISSN 0006-2960
PubMed: 16460018
DOI: 10.1021/BI0520479